Our development of algorithms for molecular modeling of protein structure is at the center of Rosetta, a powerful discovery engine that has largely cracked the “protein folding code”. My group was the first to accurately produce a fully de novo designed protein, “Top7”. We then designed an enzyme to perform the Diels-Alder reaction, a reaction not performed by any naturally occurring protein. In the last few years,our lab showed that Rosetta could be used to accurately design a whole new world of hyperstable peptides ranging in size from 8 residue cyclic peptides to mega-dalton self-assembling architectures, all with near atomic level accuracy. The increasingly complex implementations of Rosetta have had an enormous impact on protein structure prediction, which culminated in our January 2017 Science publication on large-scale structure determination using Rosetta to transform structural constraints derived from metagenomics DNA sequence data into resolved protein folds.

Awards and Achievements

  • Howard Hughes Medical Institute
  • National Academy of Sciences